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Article

Crosslinking of low-affinity glycoprotein ligands to galectin LEC-1 using a photoactivatable sulfhydryl reagent.

Biochemical and biophysical research communications - 10 Nov 2006

Arata Yoichiro, Tamura Mayumi, Nonaka Takamasa, Kasai Ken-ichi

Abstract excerpt

The N-terminal lectin domain (Nh) of the tandem repeat-type nematode galectin LEC-1 has a lower affinity for sugars than the C-terminal lectin domain. To confirm that LEC-1 forms a complex with N-acetyllactosamine-containing glycoproteins, we used several mutants of LEC-1 in which a unique cysteine residue was introduced into the Nh domain and examined their binding to bovine asialofetuin with a photoactivatable...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 16996027
DOI: 10.1016/j.bbrc.2006.09.017

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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